PRX5_HAEIN
ID PRX5_HAEIN Reviewed; 241 AA.
AC P44758;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Hybrid peroxiredoxin hyPrx5;
DE EC=1.11.1.27 {ECO:0000269|PubMed:12606554, ECO:0000269|Ref.3};
DE AltName: Full=Glutathione-dependent peroxidase {ECO:0000303|Ref.3};
DE AltName: Full=Glutathione-dependent peroxiredoxin {ECO:0000305};
DE AltName: Full=Peroxiredoxin-glutaredoxin fusion protein;
DE Short=PGdx;
DE Short=Prx-Grx;
GN Name=PGdx; OrderedLocusNames=HI_0572;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RA Hwang Y.-S., Chae H.-Z., Kim K.-H.;
RT "Characterization of Haemophilus influenzae peroxiredoxins.";
RL J. Biochem. Mol. Biol. 33:514-518(2000).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP AND MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=12606554; DOI=10.1074/jbc.m300157200;
RA Pauwels F., Vergauwen B., Vanrobaeys F., Devreese B., Van Beeumen J.J.;
RT "Purification and characterization of a chimeric enzyme from Haemophilus
RT influenzae Rd that exhibits glutathione-dependent peroxidase activity.";
RL J. Biol. Chem. 278:16658-16666(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=12529327; DOI=10.1074/jbc.m209553200;
RA Kim S.J., Woo J.R., Hwang Y.S., Jeong D.G., Shin D.H., Kim K., Ryu S.E.;
RT "The tetrameric structure of Haemophilus influenza hybrid Prx5 reveals
RT interactions between electron donor and acceptor proteins.";
RL J. Biol. Chem. 278:10790-10798(2003).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. {ECO:0000269|PubMed:12606554,
CC ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione
CC disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58297; EC=1.11.1.27;
CC Evidence={ECO:0000269|PubMed:12606554, ECO:0000269|Ref.3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.29 uM for H(2)O(2) {ECO:0000269|PubMed:12606554};
CC KM=208.8 uM for tert-butyl hydroperoxide
CC {ECO:0000269|PubMed:12606554};
CC Vmax=25.74 umol/min/mg enzyme for H(2)O(2)
CC {ECO:0000269|PubMed:12606554};
CC Vmax=26.57 umol/min/mg enzyme for tert-butyl hydroperoxide
CC {ECO:0000269|PubMed:12606554};
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:12606554};
CC -!- SUBUNIT: Homotetramer; interconnecting Prx and Grx domains of different
CC monomers. {ECO:0000269|PubMed:12529327}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In the hybrid
CC peroxiredoxin hyPrx5, no C(R) is present and C(P) instead is reduced
CC directly by the redox-active site in the Grx-domain of another monomer,
CC regenerating peroxidase activity of the enzyme. The oxidized
CC glutaredoxin is reduced by reduced glutathione (GSH) (Probable). C(P)
CC may also be reactivated by glutathionylation and subsequent reduction
CC by the Grx-domain (Probable). {ECO:0000305|PubMed:12529327,
CC ECO:0000305|PubMed:12606554}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the peroxiredoxin
CC family. Prx5 subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the glutaredoxin
CC family. {ECO:0000305}.
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DR EMBL; L42023; AAC22230.1; -; Genomic_DNA.
DR PIR; I64154; I64154.
DR RefSeq; NP_438729.1; NC_000907.1.
DR RefSeq; WP_005694168.1; NC_000907.1.
DR PDB; 1NM3; X-ray; 2.80 A; A/B=1-241.
DR PDBsum; 1NM3; -.
DR AlphaFoldDB; P44758; -.
DR SMR; P44758; -.
DR STRING; 71421.HI_0572; -.
DR PeroxiBase; 4786; HinPrxGrx_KW20.
DR EnsemblBacteria; AAC22230; AAC22230; HI_0572.
DR KEGG; hin:HI_0572; -.
DR PATRIC; fig|71421.8.peg.592; -.
DR eggNOG; COG0678; Bacteria.
DR eggNOG; COG0695; Bacteria.
DR HOGENOM; CLU_072440_2_2_6; -.
DR OMA; SFCAKAK; -.
DR PhylomeDB; P44758; -.
DR BioCyc; HINF71421:G1GJ1-584-MON; -.
DR BRENDA; 1.11.1.27; 2529.
DR EvolutionaryTrace; P44758; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR CDD; cd03013; PRX5_like; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011906; Glutaredoxin_dom.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PTHR10430; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF08534; Redoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02190; GlrX-dom; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..241
FT /note="Hybrid peroxiredoxin hyPrx5"
FT /id="PRO_0000056612"
FT DOMAIN 3..167
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 170..241
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT ACT_SITE 49
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxiredoxin activity"
FT /evidence="ECO:0000305|PubMed:12606554"
FT DISULFID 180..183
FT /note="Redox-active; for glutaredoxin activity"
FT /evidence="ECO:0000269|PubMed:12529327"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1NM3"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:1NM3"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:1NM3"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:1NM3"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1NM3"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1NM3"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1NM3"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1NM3"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1NM3"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:1NM3"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1NM3"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1NM3"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:1NM3"
SQ SEQUENCE 241 AA; 26743 MW; D2FD230D20BE63F0 CRC64;
MSSMEGKKVP QVTFRTRQGD KWVDVTTSEL FDNKTVIVFS LPGAFTPTCS SSHLPRYNEL
APVFKKYGVD DILVVSVNDT FVMNAWKEDE KSENISFIPD GNGEFTEGMG MLVGKEDLGF
GKRSWRYSML VKNGVVEKMF IEPNEPGDPF KVSDADTMLK YLAPQHQVQE SISIFTKPGC
PFCAKAKQLL HDKGLSFEEI ILGHDATIVS VRAVSGRTTV PQVFIGGKHI GGSDDLEKYF
A
